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Protein

Basic salivary proline-rich protein 3

Gene

PRB3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a receptor for the Gram-negative bacterium F.nucleatum.1 Publication

GO - Biological processi

  • defense response to Gram-negative bacterium Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Basic salivary proline-rich protein 3
Alternative name(s):
Parotid salivary glycoprotein G1
Proline-rich protein G1
Gene namesi
Name:PRB3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:9339. PRB3.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33701.

Polymorphism and mutation databases

BioMutaiPRB3.
DMDMi229462763.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1616Sequence analysisAdd
BLAST
Chaini17 – 309293Basic salivary proline-rich protein 3PRO_0000022097Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei17 – 171Pyrrolidone carboxylic acid1 Publication
Modified residuei24 – 241Phosphoserine1 Publication
Glycosylationi66 – 661N-linked (GlcNAc...)Sequence analysis
Glycosylationi87 – 871N-linked (GlcNAc...); prevalent in head and neck cancer patients1 Publication
Glycosylationi89 – 891O-linked (Hex)1 Publication
Glycosylationi108 – 1081N-linked (GlcNAc...)Sequence analysis
Glycosylationi129 – 1291N-linked (GlcNAc...)Sequence analysis
Glycosylationi150 – 1501N-linked (GlcNAc...)Sequence analysis
Glycosylationi171 – 1711N-linked (GlcNAc...)Sequence analysis
Glycosylationi192 – 1921N-linked (GlcNAc...)Sequence analysis
Glycosylationi213 – 2131N-linked (GlcNAc...)Sequence analysis
Glycosylationi255 – 2551N-linked (GlcNAc...); atypical1 Publication

Post-translational modificationi

The Gl-8 variant contains an interchain disulfide bond with salivary peroxidase.
N- and O-glycosylated; contains about 50% carbohydrate. This is composed of highly fucosylated N-linked saccharides, the major structure is a biantennary asialosaccharide containing 2 fucose residues on one antenna and an unsubstituted terminal lactosamine sequence on the other. The Gram-negative bacterium F.nucleatum binds to carbohydrates containing unsubstituted GalBeta1,4GlcNAc residues.2 Publications
Proteolytically cleaved at the tripeptide Xaa-Pro-Gln, where Xaa in the P3 position is mostly lysine. The endoprotease may be of microbial origin. Besides on the N-terminal of mature PRB3, pyroglutamate formation found on at least Gln-67, Gln-88, Gln-214 and Gln-295.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PRIDEiQ04118.
TopDownProteomicsiQ04118.

PTM databases

iPTMnetiQ04118.

Expressioni

Gene expression databases

BgeeiQ04118.
CleanExiHS_PRB3.
ExpressionAtlasiQ04118. baseline and differential.
GenevisibleiQ04118. HS.

Interactioni

Subunit structurei

The Gl-8 variant forms a disulfide-bonded heterodimer with salivary perodixase.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati53 – 73211Add
BLAST
Repeati74 – 94212Add
BLAST
Repeati95 – 115213Add
BLAST
Repeati116 – 136214Add
BLAST
Repeati137 – 157215Add
BLAST
Repeati158 – 178216Add
BLAST
Repeati179 – 199217Add
BLAST
Repeati200 – 220218Add
BLAST
Repeati221 – 241219Add
BLAST
Repeati242 – 2622110Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni53 – 26221010 X 21 AA tandem repeats of [RH]-P-G-K-P-[EQ]-G-[PQS]-P-[PS]-Q-[GE]-G-N-[QK]-[SP]-[QR]-[GR]-P-P-PAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi36 – 308273Pro-richAdd
BLAST

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

HOGENOMiHOG000060075.
InParanoidiQ04118.

Family and domain databases

InterProiIPR026086. Pro-rich.
[Graphical view]
PANTHERiPTHR23203. PTHR23203. 1 hit.
PfamiPF15240. Pro-rich. 6 hits.
[Graphical view]
SMARTiSM01412. Pro-rich. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q04118-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLILLSVAL LALSSAQSLN EDVSQEESPS VISGKPEGRR PQGGNQPQRT
60 70 80 90 100
PPPPGKPEGR PPQGGNQSQG PPPRPGKPEG PPPQGGNQSQ GPPPRPGKPE
110 120 130 140 150
GQPPQGGNQS QGPPPRPGKP EGPPPQGGNQ SQGPPPRPGK PEGPPPQGGN
160 170 180 190 200
QSQGPPPHPG KPEGPPPQGG NQSQGPPPRP GKPEGPPPQG GNQSQGPPPR
210 220 230 240 250
PGKPEGPPPQ GGNQSQGPPP RPGKPEGSPS QGGNKPQGPP PHPGKPQGPP
260 270 280 290 300
PQEGNKPQRP PPPGRPQGPP PPGGNPQQPL PPPAGKPQGP PPPPQGGRPH

RPPQGQPPQ
Length:309
Mass (Da):30,980
Last modified:May 5, 2009 - v2
Checksum:iA8FCBEBA784618C6
GO

Sequence cautioni

The sequence CAA30477.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401R → P in CAA30728 (PubMed:2851479).Curated
Sequence conflicti47 – 537PQRTPPP → SQGPPPR in CAA30728 (PubMed:2851479).Curated
Sequence conflicti51 – 511P → S in CAA30477 (PubMed:2851479).Curated
Sequence conflicti60 – 601R → P in CAA30728 (PubMed:2851479).Curated
Sequence conflicti81 – 811P → Q in CAA30728 (PubMed:2851479).Curated
Sequence conflicti102 – 1021Q → P in CAA30728 (PubMed:2851479).Curated
Sequence conflicti119 – 1191K → E in CAA30728 (PubMed:2851479).Curated
Sequence conflicti137 – 1371R → H in CAA30728 (PubMed:2851479).Curated
Sequence conflicti158 – 1581H → R in CAA30728 (PubMed:2851479).Curated
Sequence conflicti158 – 1581H → R in AAH96211 (PubMed:15489334).Curated
Sequence conflicti237 – 2371Q → R in CAA30728 (PubMed:2851479).Curated
Sequence conflicti264 – 2641G → R in CAA30728 (PubMed:2851479).Curated
Sequence conflicti264 – 2641G → R in CAA30477 (PubMed:2851479).Curated

Polymorphismi

The number of repeats is polymorphic and varies among different alleles. The sequence shown is that of allele L (long). There is an allele S (short) which contains 6 tandem repeats.1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti53 – 531P → C in Gl-8; requires 2 nucleotide substitutions. 1 Publication
VAR_019696
Natural varianti158 – 22063Missing in allele S.
VAR_055031Add
BLAST
Natural varianti186 – 1861P → Q.1 Publication
Corresponds to variant rs11054208 [ dbSNP | Ensembl ].
VAR_055032

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07637 Genomic DNA. Translation: CAA30477.1. Sequence problems.
X07881 Genomic DNA. Translation: CAA30728.1.
BC096209 mRNA. Translation: AAH96209.1.
BC096210 mRNA. Translation: AAH96210.1.
BC096211 mRNA. Translation: AAH96211.1.
PIRiA36298.
B36298.
S10889.
UniGeneiHs.73031.

Genome annotation databases

EnsembliENST00000381842; ENSP00000371264; ENSG00000197870.
UCSCiuc058lgs.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07637 Genomic DNA. Translation: CAA30477.1. Sequence problems.
X07881 Genomic DNA. Translation: CAA30728.1.
BC096209 mRNA. Translation: AAH96209.1.
BC096210 mRNA. Translation: AAH96210.1.
BC096211 mRNA. Translation: AAH96211.1.
PIRiA36298.
B36298.
S10889.
UniGeneiHs.73031.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiQ04118.

Polymorphism and mutation databases

BioMutaiPRB3.
DMDMi229462763.

Proteomic databases

PRIDEiQ04118.
TopDownProteomicsiQ04118.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000381842; ENSP00000371264; ENSG00000197870.
UCSCiuc058lgs.1. human.

Organism-specific databases

GeneCardsiPRB3.
H-InvDBHIX0201930.
HGNCiHGNC:9339. PRB3.
MIMi168840. gene.
neXtProtiNX_Q04118.
PharmGKBiPA33701.
GenAtlasiSearch...

Phylogenomic databases

HOGENOMiHOG000060075.
InParanoidiQ04118.

Miscellaneous databases

PROiQ04118.
SOURCEiSearch...

Gene expression databases

BgeeiQ04118.
CleanExiHS_PRB3.
ExpressionAtlasiQ04118. baseline and differential.
GenevisibleiQ04118. HS.

Family and domain databases

InterProiIPR026086. Pro-rich.
[Graphical view]
PANTHERiPTHR23203. PTHR23203. 1 hit.
PfamiPF15240. Pro-rich. 6 hits.
[Graphical view]
SMARTiSM01412. Pro-rich. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Length polymorphisms in human proline-rich protein genes generated by intragenic unequal crossing over."
    Lyons K.M., Stein J.H., Smithies O.
    Genetics 120:267-278(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES L AND S), POLYMORPHISM.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE L), VARIANT GLN-186.
  3. "Alleles at the PRB3 locus coding for a disulfide-bonded human salivary proline-rich glycoprotein (Gl 8) and a null in an Ashkenazi Jew."
    Azen E.A., Minaguchi K., Latreille P., Kim H.-S.
    Am. J. Hum. Genet. 47:686-697(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-309 (ALLELE S), VARIANT GL-8 CYS-53, INTERACTION WITH SALIVARY PEROXIDASE, DISULFIDE BOND.
  4. "Structure and bacterial receptor activity of a human salivary proline-rich glycoprotein."
    Gillece-Castro B.L., Prakobphol A., Burlingame A.L., Leffler H., Fisher S.J.
    J. Biol. Chem. 266:17358-17368(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 68-92; 110-127; 131-148; 173-190 AND 194-211, FUNCTION, GLYCOSYLATION.
    Tissue: Saliva.
  5. "Identification of Lys-Pro-Gln as a novel cleavage site specificity of saliva-associated proteases."
    Helmerhorst E.J., Sun X., Salih E., Oppenheim F.G.
    J. Biol. Chem. 283:19957-19966(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "Finding new posttranslational modifications in salivary proline-rich proteins."
    Vitorino R., Alves R., Barros A., Caseiro A., Ferreira R., Lobo M.C., Bastos A., Duarte J., Carvalho D., Santos L.L., Amado F.L.
    Proteomics 10:3732-3742(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-87; SER-89 AND ASN-255, PYROGLUTAMATE FORMATION AT GLN-17, PHOSPHORYLATION AT SER-24, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiPRB3_HUMAN
AccessioniPrimary (citable) accession number: Q04118
Secondary accession number(s): Q15188
, Q4VAY3, Q4VAY4, Q7M4M9, Q9UCT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: May 5, 2009
Last modified: June 8, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.